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Erratum to 'Proteomic analysis of differential protein expression in Acidithiobacillus ferrooxidans cultivated in high potassium concentration' [Microbiol. Res. 168 (7) (2013) 455–460]

Authors :
Bo Li
Huijun Zhang
Jianping Ouyang
Xinhua Chen
Li Gu
Wenbin Guo
Source :
Microbiological Research. 182:163-168
Publication Year :
2016
Publisher :
Elsevier BV, 2016.

Abstract

Acidithiobacillus ferrooxidans is a chemolithoautotrophic acidophile that oxidizes ferrous iron or sulfur compounds to obtain energy in the presence of various ions. To investigate the potassium ion response of A. ferrooxidans, we conducted a proteomics analysis. We identified eight proteins that were differentially expressed in the presence of high potassium concentration, including four up-regulated and four down-regulated proteins. Transcription levels of the genes encoding differential expressed proteins were subsequently analyzed by Northern blot in the presence of high potassium concentration. Among the up-regulated proteins, GDP-mannose 4,6-dehydratase, ribose 5-phosphate isomerase A and ribose-phosphate pyrophosphokinase were known to be implicated in the synthesis of glycocalyx, suggesting that the formation of glycocalyx might be involved in the A. ferrooxidans response to high potassium concentration. Thickening of the glycocalyx layer was also observed in cells cultivated under high potassium concentration via transmission electronic microscopy (TEM) analysis. Among the down-regulated proteins, ATP synthase F1 delta subunit and ATP synthase F1 beta subunit were two important components of ATP synthase. ATP synthase (P-ATPase) is directly linked to the transport of potassium into the cell, thus Acidithiobacillus ferrooxidans might just reduce the quantity of ATP synthase to offset the high potassium level in the culture medium. Therefore, the results obtained here provide some new clues to improve our understanding of the response of A. ferrooxidans to high potassium concentration.

Details

ISSN :
09445013
Volume :
182
Database :
OpenAIRE
Journal :
Microbiological Research
Accession number :
edsair.doi.dedup.....fbb5a9820da74876653e71c1a3f83d6e
Full Text :
https://doi.org/10.1016/j.micres.2015.02.004